Determination of the course of the chain of globular proteins by the self-consistent field method

It is shown that calculation of the thermodynamically stable packing of the protein chain in a domain or in a small globule may be an encompassable task. As an example the search for the most stable packings for amino acid sequences of two β-structural proteins is considered. The approach proposed is based on two physical ideas: 1) use of the molecular field method for organizing an effective sorting of a huge multiplicity of similar structures; and 2) limitation of the set of structures considered solely to those packings of the chain which may prove stable at least for a certain amino acid sequence.